BMRB Entry 25576

Assembly:

Entities:

Entity 1, human SUMO1 111 residues - 11149.640 Da.

Residues 1-14 (MGSSHHHHHHSQDP) represent a non-native purification tag. These residues were neither assigned nor included in structure calculation.

Samples:

CN: SUMO1, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

N: SUMO1, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

Phage: SUMO1, [U-100% 15N], 0.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; Pf1 phage 10 ± 0.1 w/v; H2O 90%; D2O 10%

Unlabeled: SUMO10.5 – 1 mM; potassium phosphate 10 ± 1 mM; potassium chloride 100 ± 1 mM; DTT 2 ± 0.05 mM; EDTA 0.1 ± 0.005 mM; sodium azide 0.001 ± 0.001 %; H2O 90%; D2O 10%

Default: pH: 6.5; pressure: 1 atm; temperature: 290 K

Experiments:

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking

CYANA v3.9, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

• Bruker Avance 500 MHz
• Bruker Avance 600 MHz
• Bruker Avance 800 MHz
• Bruker Avance 850 MHz